about
Structural modification of pantothenamides counteracts degradation by pantetheinase and improves antiplasmodial activityA class of pantothenic acid analogs inhibits Plasmodium falciparum pantothenate kinase and represses the proliferation of malaria parasitesPantothenamides are potent, on-target inhibitors of Plasmodium falciparum growth when serum pantetheinase is inactivatedCoenzyme A biosynthesis: an antimicrobial drug target.The human malaria parasite Plasmodium falciparum is not dependent on host coenzyme A biosynthesis.Exploiting the coenzyme A biosynthesis pathway for the identification of new antimalarial agents: the case for pantothenamides.A miniaturized assay for measuring small molecule phosphorylation in the presence of complex matrices.Antiplasmodial Mode of Action of Pantothenamides: Pantothenate Kinase Serves as a Metabolic Activator Not as a Target.Feedback inhibition of pantothenate kinase regulates pantothenol uptake by the malaria parasite.Structure-activity analysis of CJ-15,801 analogues that interact with Plasmodium falciparum pantothenate kinase and inhibit parasite proliferation.Mutations in the pantothenate kinase of Plasmodium falciparum confer diverse sensitivity profiles to antiplasmodial pantothenate analogues.Structure-activity relationships of antiplasmodial pantothenamide analogs reveal a new way by which triazoles mimic amide bondsStructural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility-mass spectrometry
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description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Christina Spry
@ast
Christina Spry
@en
Christina Spry
@es
Christina Spry
@nl
type
label
Christina Spry
@ast
Christina Spry
@en
Christina Spry
@es
Christina Spry
@nl
prefLabel
Christina Spry
@ast
Christina Spry
@en
Christina Spry
@es
Christina Spry
@nl
P106
P21
P31
P496
0000-0002-8156-7070